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Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Additionally we are shipping Sulfiredoxin 1 Antibodies (31) and Sulfiredoxin 1 Kits (3) and many more products for this protein.
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This review will summarize the molecular basis of differences in the affinity of Srx for individual Prx (show PRDX6 Proteins) and the role of individual component of the Srx-Prx (show PRDX6 Proteins) system in tumor progression and metastasis.
Gemfibrozil, a lipid-lowering drug, increases myelin genes in human oligodendrocytes via peroxisome proliferator-activated receptor-beta (show PPARD Proteins).
NRF2 (show GABPA Proteins) and SRXN1 genetic polymorphisms are associated with breast cancer risk and survival
SRX forms a complex with S100A4 (show S100A4 Proteins) (and has stronger affinity for S-glutathionylated S100A4 (show S100A4 Proteins)), regulates its activity, and mediates redox regulation of the interaction of S100A4 (show S100A4 Proteins) with nonmuscle myosin heavy chain II-A (show MYH9 Proteins).
Srx functions as a novel component to maintain the balance between H2O2 production and elimination
Real-time PCR validated that up-regulation of sulphiredoxin 1 homolog (SRXN1), hemeoxygenase 1 (HMOX1), and breast carcinoma amplified sequence 3 (BCAS3) were consistently modulated.
Srx-Prx IV (show PRDX4 Proteins) axis is critical for lung cancer maintenance and metastasis, suggesting that targeting the Srx-Prx IV (show PRDX4 Proteins) axis may provide unique effective strategies for cancer prevention and treatment.
sulfiredoxin 1 is associatd with the pathogenesis of human pulmonary fibrosis.
Studies present the 2.1 A crystal structure of human Srx in complex with PrxI (show PRDX1 Proteins), ATP, and Mg(2 (show MUC7 Proteins)+).
The reduction of the cysteine sulfinic acid moiety within the active site of the peroxiredoxin by sulfiredoxin involves novel sulfur chemistry and the use of ATP and Mg(2 (show MUC7 Proteins)+).
sulfiredoxin is degraded by Lon (show LONP1 Proteins) in a manner dependent on PrxIII (show PRDX3 Proteins) hyperoxidation state.
Srx is one of the critical components that contribute to mouse skin tumorigenesis in vivo.
data provide in vivo evidence that loss of Srx renders mice resistant to azoxymethane/dextran sulfate sodium-induced colon carcinogenesis, suggesting that Srx has a critical oncogenic role in cancer development
The concerted action of PrxIII (show PRDX3 Proteins) and Srx is important for protection against pyrazole-induced oxidative stress arising from the convergent induction of CYP2E1 (show CYP2E1 Proteins)-derived and ER stress-derived ROS (show ROS1 Proteins) in mitochondria.
NO-mediated Srx up-regulation is mediated by the transcription factor nuclear factor erythroid 2-related factor (Nrf2 (show NFE2L2 Proteins)) and the NO/Srx pathway inhibits generation of reactive oxygen species.
LPS (show TLR4 Proteins)-mediated Srx induction is dependent on both AP-1 (show JUN Proteins) and Nrf2 (show NFE2L2 Proteins), which is regulated by Nox2 (show CYBB Proteins)-derived reactive oxygen species.
Synaptic activity upregulated the thioredoxin (show TXN Proteins)-peroxiredoxin reactivating gene sulfiredoxin.
Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or PRDX6. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and a thioltransferase.
, sulfiredoxin 1 homolog
, sulfiredoxin 1 homolog (S. cerevisiae)
, neoplastic progression 3
, neoplastic progression protein 3